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Database: PDB
Entry: 4M66
LinkDB: 4M66
Original site: 4M66 
HEADER    TRANSFERASE                             09-AUG-13   4M66              
TITLE     CRYSTAL STRUCTURE OF THE MOUSE RIP3 KINASE DOMAIN                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RECEPTOR-INTERACTING SERINE/THREONINE-PROTEIN KINASE 3;    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 1-313;                                        
COMPND   5 SYNONYM: RIP-LIKE PROTEIN KINASE 3, RECEPTOR-INTERACTING PROTEIN 3,  
COMPND   6 RIP-3, MRIP3;                                                        
COMPND   7 EC: 2.7.11.1;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: RIPK3;                                                         
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    KINASE, PROTEIN PHOSPHORYLATION, TRANSFERASE                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.XIE,W.PENG,C.YAN,J.WU,Y.SHI                                         
REVDAT   2   06-NOV-13 4M66    1       JRNL                                     
REVDAT   1   16-OCT-13 4M66    0                                                
JRNL        AUTH   T.XIE,W.PENG,C.YAN,J.WU,X.GONG,Y.SHI                         
JRNL        TITL   STRUCTURAL INSIGHTS INTO RIP3-MEDIATED NECROPTOTIC SIGNALING 
JRNL        REF    CELL REP                      V.   5    70 2013              
JRNL        REFN                   ESSN 2211-1247                               
JRNL        PMID   24095729                                                     
JRNL        DOI    10.1016/J.CELREP.2013.08.044                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.3_928)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.89                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 24065                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.217                           
REMARK   3   R VALUE            (WORKING SET) : 0.215                           
REMARK   3   FREE R VALUE                     : 0.258                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.080                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1222                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 35.8919 -  4.9904    0.98     2658   129  0.1989 0.2473        
REMARK   3     2  4.9904 -  3.9627    0.99     2591   143  0.1803 0.2217        
REMARK   3     3  3.9627 -  3.4622    0.85     2196   124  0.2127 0.2345        
REMARK   3     4  3.4622 -  3.1459    1.00     2579   141  0.2329 0.2675        
REMARK   3     5  3.1459 -  2.9205    1.00     2576   156  0.2373 0.2998        
REMARK   3     6  2.9205 -  2.7484    1.00     2566   129  0.2411 0.2969        
REMARK   3     7  2.7484 -  2.6108    1.00     2569   148  0.2596 0.3114        
REMARK   3     8  2.6108 -  2.4972    0.99     2549   124  0.2583 0.2699        
REMARK   3     9  2.4972 -  2.4011    0.99     2559   128  0.2540 0.3157        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.20                                          
REMARK   3   SHRINKAGE RADIUS   : 0.98                                          
REMARK   3   K_SOL              : 0.32                                          
REMARK   3   B_SOL              : 40.83                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.340            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.700           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 42.36                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 55.55                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 12.97200                                             
REMARK   3    B22 (A**2) : 2.98450                                              
REMARK   3    B33 (A**2) : -7.51100                                             
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : -10.64620                                            
REMARK   3    B23 (A**2) : -0.00000                                             
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008           4286                                  
REMARK   3   ANGLE     :  1.161           5821                                  
REMARK   3   CHIRALITY :  0.076            659                                  
REMARK   3   PLANARITY :  0.006            744                                  
REMARK   3   DIHEDRAL  : 15.826           1584                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  17.3987   7.2450 -19.7831              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2945 T22:   0.3266                                     
REMARK   3      T33:   0.2966 T12:   0.0618                                     
REMARK   3      T13:   0.0059 T23:   0.0436                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6365 L22:   0.7438                                     
REMARK   3      L33:   2.0538 L12:   0.2383                                     
REMARK   3      L13:   0.5567 L23:  -0.0497                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0699 S12:   0.0604 S13:  -0.1387                       
REMARK   3      S21:  -0.0012 S22:  -0.1221 S23:  -0.2482                       
REMARK   3      S31:   0.1290 S32:   0.5306 S33:   0.0258                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4M66 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-AUG-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB081515.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-OCT-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9796                             
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24093                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4ITH                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.35                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05M MAGNESIUM FORMATE, 13% PEG 3350,   
REMARK 280  PH 7, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       77.61200            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       25.81700            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       77.61200            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       25.81700            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     VAL A     4                                                      
REMARK 465     LYS A     5                                                      
REMARK 465     LEU A     6                                                      
REMARK 465     TRP A     7                                                      
REMARK 465     PRO A     8                                                      
REMARK 465     THR A     9                                                      
REMARK 465     GLY A    10                                                      
REMARK 465     ALA A    11                                                      
REMARK 465     SER A    12                                                      
REMARK 465     ALA A    13                                                      
REMARK 465     VAL A    14                                                      
REMARK 465     SER A   171                                                      
REMARK 465     GLN A   172                                                      
REMARK 465     SER A   173                                                      
REMARK 465     GLY A   174                                                      
REMARK 465     SER A   175                                                      
REMARK 465     GLY A   176                                                      
REMARK 465     SER A   177                                                      
REMARK 465     GLY A   178                                                      
REMARK 465     SER A   179                                                      
REMARK 465     GLY A   180                                                      
REMARK 465     SER A   181                                                      
REMARK 465     ARG A   182                                                      
REMARK 465     ASP A   183                                                      
REMARK 465     SER A   184                                                      
REMARK 465     GLY A   185                                                      
REMARK 465     LYS A   198                                                      
REMARK 465     VAL A   199                                                      
REMARK 465     ASN A   200                                                      
REMARK 465     LYS A   230                                                      
REMARK 465     THR A   231                                                      
REMARK 465     SER A   232                                                      
REMARK 465     LEU A   233                                                      
REMARK 465     ILE A   234                                                      
REMARK 465     ARG A   235                                                      
REMARK 465     GLU A   236                                                      
REMARK 465     THR A   237                                                      
REMARK 465     VAL A   238                                                      
REMARK 465     CYS A   239                                                      
REMARK 465     ASP A   240                                                      
REMARK 465     ARG A   241                                                      
REMARK 465     HIS A   313                                                      
REMARK 465     LEU A   314                                                      
REMARK 465     GLU A   315                                                      
REMARK 465     HIS A   316                                                      
REMARK 465     HIS A   317                                                      
REMARK 465     HIS A   318                                                      
REMARK 465     HIS A   319                                                      
REMARK 465     HIS A   320                                                      
REMARK 465     HIS A   321                                                      
REMARK 465     HIS A   322                                                      
REMARK 465     HIS A   323                                                      
REMARK 465     HIS A   324                                                      
REMARK 465     HIS A   325                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     VAL B     4                                                      
REMARK 465     LYS B     5                                                      
REMARK 465     LEU B     6                                                      
REMARK 465     TRP B     7                                                      
REMARK 465     PRO B     8                                                      
REMARK 465     THR B     9                                                      
REMARK 465     GLY B    10                                                      
REMARK 465     ALA B    11                                                      
REMARK 465     SER B    12                                                      
REMARK 465     ALA B    13                                                      
REMARK 465     GLY B   169                                                      
REMARK 465     GLY B   170                                                      
REMARK 465     SER B   171                                                      
REMARK 465     GLN B   172                                                      
REMARK 465     SER B   173                                                      
REMARK 465     GLY B   174                                                      
REMARK 465     SER B   175                                                      
REMARK 465     GLY B   176                                                      
REMARK 465     SER B   177                                                      
REMARK 465     GLY B   178                                                      
REMARK 465     SER B   179                                                      
REMARK 465     GLY B   180                                                      
REMARK 465     SER B   181                                                      
REMARK 465     ARG B   182                                                      
REMARK 465     ASP B   183                                                      
REMARK 465     SER B   184                                                      
REMARK 465     GLY B   185                                                      
REMARK 465     GLY B   186                                                      
REMARK 465     THR B   187                                                      
REMARK 465     LYS B   198                                                      
REMARK 465     VAL B   199                                                      
REMARK 465     ASN B   200                                                      
REMARK 465     ASP B   229                                                      
REMARK 465     LYS B   230                                                      
REMARK 465     THR B   231                                                      
REMARK 465     SER B   232                                                      
REMARK 465     LEU B   233                                                      
REMARK 465     ILE B   234                                                      
REMARK 465     ARG B   235                                                      
REMARK 465     GLU B   236                                                      
REMARK 465     THR B   237                                                      
REMARK 465     VAL B   238                                                      
REMARK 465     CYS B   239                                                      
REMARK 465     ASP B   240                                                      
REMARK 465     ARG B   241                                                      
REMARK 465     LEU B   314                                                      
REMARK 465     GLU B   315                                                      
REMARK 465     HIS B   316                                                      
REMARK 465     HIS B   317                                                      
REMARK 465     HIS B   318                                                      
REMARK 465     HIS B   319                                                      
REMARK 465     HIS B   320                                                      
REMARK 465     HIS B   321                                                      
REMARK 465     HIS B   322                                                      
REMARK 465     HIS B   323                                                      
REMARK 465     HIS B   324                                                      
REMARK 465     HIS B   325                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A 110    CG   CD   OE1  OE2                                  
REMARK 470     PHE A 197    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU A 201    CG   CD1  CD2                                       
REMARK 470     LYS A 202    CG   CD   CE   NZ                                   
REMARK 470     ASP A 229    CG   OD1  OD2                                       
REMARK 470     GLU B 110    CG   CD   OE1  OE2                                  
REMARK 470     PHE B 197    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU B 201    CG   CD1  CD2                                       
REMARK 470     LYS B 202    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    ARG B    96     O    HOH B   408              1.91            
REMARK 500   NH2  ARG B    19     O    HOH B   405              2.04            
REMARK 500   O    HOH A   443     O    HOH A   451              2.14            
REMARK 500   OE2  GLU A   290     O    HOH A   484              2.15            
REMARK 500   O    HOH A   447     O    HOH A   454              2.15            
REMARK 500   O    HOH A   407     O    HOH A   457              2.16            
REMARK 500   N    GLN A    84     O    HOH A   423              2.17            
REMARK 500   O    CYS A   119     O    HOH A   409              2.18            
REMARK 500   O    ARG A   142     O    HOH A   436              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A  25     -149.57   -114.42                                   
REMARK 500    ASN A  70      144.67   -172.32                                   
REMARK 500    ASP A  86       40.48     39.87                                   
REMARK 500    GLU A 110       30.95    -91.74                                   
REMARK 500    ARG A 142       -8.59     74.08                                   
REMARK 500    ASP A 161       79.95     66.14                                   
REMARK 500    THR A 187       -3.77    -46.37                                   
REMARK 500    PRO A 258      -93.91    -38.39                                   
REMARK 500    LEU B  25     -155.83   -119.88                                   
REMARK 500    LYS B  30     -161.35    -70.93                                   
REMARK 500    SER B  55        2.32    -64.53                                   
REMARK 500    ASN B  70      141.85   -174.88                                   
REMARK 500    ASP B  86       28.92     43.14                                   
REMARK 500    PHE B  87       -4.99     92.76                                   
REMARK 500    ARG B 142       -8.87     73.84                                   
REMARK 500    LEU B 155       30.82     76.92                                   
REMARK 500    ASP B 161       97.00     61.10                                   
REMARK 500    GLU B 224      176.87    -52.78                                   
REMARK 500    LEU B 227       58.47   -119.99                                   
REMARK 500    PRO B 251      151.31    -48.60                                   
REMARK 500    PRO B 258     -107.12    -33.34                                   
REMARK 500    LYS B 298       22.37   -141.10                                   
REMARK 500    SER B 311       31.13    -59.85                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4M67   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4M68   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4M69   RELATED DB: PDB                                   
DBREF  4M66 A    1   313  UNP    Q9QZL0   RIPK3_MOUSE      1    313             
DBREF  4M66 B    1   313  UNP    Q9QZL0   RIPK3_MOUSE      1    313             
SEQADV 4M66 ALA A  111  UNP  Q9QZL0    CYS   111 ENGINEERED MUTATION            
SEQADV 4M66 LEU A  314  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 4M66 GLU A  315  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 4M66 HIS A  316  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 4M66 HIS A  317  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 4M66 HIS A  318  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 4M66 HIS A  319  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 4M66 HIS A  320  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 4M66 HIS A  321  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 4M66 HIS A  322  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 4M66 HIS A  323  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 4M66 HIS A  324  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 4M66 HIS A  325  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 4M66 ALA B  111  UNP  Q9QZL0    CYS   111 ENGINEERED MUTATION            
SEQADV 4M66 LEU B  314  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 4M66 GLU B  315  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 4M66 HIS B  316  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 4M66 HIS B  317  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 4M66 HIS B  318  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 4M66 HIS B  319  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 4M66 HIS B  320  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 4M66 HIS B  321  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 4M66 HIS B  322  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 4M66 HIS B  323  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 4M66 HIS B  324  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 4M66 HIS B  325  UNP  Q9QZL0              EXPRESSION TAG                 
SEQRES   1 A  325  MET SER SER VAL LYS LEU TRP PRO THR GLY ALA SER ALA          
SEQRES   2 A  325  VAL PRO LEU VAL SER ARG GLU GLU LEU LYS LYS LEU GLU          
SEQRES   3 A  325  PHE VAL GLY LYS GLY GLY PHE GLY VAL VAL PHE ARG ALA          
SEQRES   4 A  325  HIS HIS ARG THR TRP ASN HIS ASP VAL ALA VAL LYS ILE          
SEQRES   5 A  325  VAL ASN SER LYS LYS ILE SER TRP GLU VAL LYS ALA MET          
SEQRES   6 A  325  VAL ASN LEU ARG ASN GLU ASN VAL LEU LEU LEU LEU GLY          
SEQRES   7 A  325  VAL THR GLU ASP LEU GLN TRP ASP PHE VAL SER GLY GLN          
SEQRES   8 A  325  ALA LEU VAL THR ARG PHE MET GLU ASN GLY SER LEU ALA          
SEQRES   9 A  325  GLY LEU LEU GLN PRO GLU ALA PRO ARG PRO TRP PRO LEU          
SEQRES  10 A  325  LEU CYS ARG LEU LEU GLN GLU VAL VAL LEU GLY MET CYS          
SEQRES  11 A  325  TYR LEU HIS SER LEU ASP PRO PRO LEU LEU HIS ARG ASP          
SEQRES  12 A  325  LEU LYS PRO SER ASN ILE LEU LEU ASP PRO GLU LEU HIS          
SEQRES  13 A  325  ALA LYS LEU ALA ASP PHE GLY LEU SER THR PHE GLN GLY          
SEQRES  14 A  325  GLY SER GLN SER GLY SER GLY SER GLY SER GLY SER ARG          
SEQRES  15 A  325  ASP SER GLY GLY THR LEU ALA TYR LEU ASP PRO GLU LEU          
SEQRES  16 A  325  LEU PHE LYS VAL ASN LEU LYS ALA SER LYS ALA SER ASP          
SEQRES  17 A  325  VAL TYR SER PHE GLY ILE LEU VAL TRP ALA VAL LEU ALA          
SEQRES  18 A  325  GLY ARG GLU ALA GLU LEU VAL ASP LYS THR SER LEU ILE          
SEQRES  19 A  325  ARG GLU THR VAL CYS ASP ARG GLN SER ARG PRO PRO LEU          
SEQRES  20 A  325  THR GLU LEU PRO PRO GLY SER PRO GLU THR PRO GLY LEU          
SEQRES  21 A  325  GLU LYS LEU LYS GLU LEU MET ILE HIS CYS TRP GLY SER          
SEQRES  22 A  325  GLN SER GLU ASN ARG PRO SER PHE GLN ASP CYS GLU PRO          
SEQRES  23 A  325  LYS THR ASN GLU VAL TYR ASN LEU VAL LYS ASP LYS VAL          
SEQRES  24 A  325  ASP ALA ALA VAL SER GLU VAL LYS HIS TYR LEU SER GLN          
SEQRES  25 A  325  HIS LEU GLU HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS          
SEQRES   1 B  325  MET SER SER VAL LYS LEU TRP PRO THR GLY ALA SER ALA          
SEQRES   2 B  325  VAL PRO LEU VAL SER ARG GLU GLU LEU LYS LYS LEU GLU          
SEQRES   3 B  325  PHE VAL GLY LYS GLY GLY PHE GLY VAL VAL PHE ARG ALA          
SEQRES   4 B  325  HIS HIS ARG THR TRP ASN HIS ASP VAL ALA VAL LYS ILE          
SEQRES   5 B  325  VAL ASN SER LYS LYS ILE SER TRP GLU VAL LYS ALA MET          
SEQRES   6 B  325  VAL ASN LEU ARG ASN GLU ASN VAL LEU LEU LEU LEU GLY          
SEQRES   7 B  325  VAL THR GLU ASP LEU GLN TRP ASP PHE VAL SER GLY GLN          
SEQRES   8 B  325  ALA LEU VAL THR ARG PHE MET GLU ASN GLY SER LEU ALA          
SEQRES   9 B  325  GLY LEU LEU GLN PRO GLU ALA PRO ARG PRO TRP PRO LEU          
SEQRES  10 B  325  LEU CYS ARG LEU LEU GLN GLU VAL VAL LEU GLY MET CYS          
SEQRES  11 B  325  TYR LEU HIS SER LEU ASP PRO PRO LEU LEU HIS ARG ASP          
SEQRES  12 B  325  LEU LYS PRO SER ASN ILE LEU LEU ASP PRO GLU LEU HIS          
SEQRES  13 B  325  ALA LYS LEU ALA ASP PHE GLY LEU SER THR PHE GLN GLY          
SEQRES  14 B  325  GLY SER GLN SER GLY SER GLY SER GLY SER GLY SER ARG          
SEQRES  15 B  325  ASP SER GLY GLY THR LEU ALA TYR LEU ASP PRO GLU LEU          
SEQRES  16 B  325  LEU PHE LYS VAL ASN LEU LYS ALA SER LYS ALA SER ASP          
SEQRES  17 B  325  VAL TYR SER PHE GLY ILE LEU VAL TRP ALA VAL LEU ALA          
SEQRES  18 B  325  GLY ARG GLU ALA GLU LEU VAL ASP LYS THR SER LEU ILE          
SEQRES  19 B  325  ARG GLU THR VAL CYS ASP ARG GLN SER ARG PRO PRO LEU          
SEQRES  20 B  325  THR GLU LEU PRO PRO GLY SER PRO GLU THR PRO GLY LEU          
SEQRES  21 B  325  GLU LYS LEU LYS GLU LEU MET ILE HIS CYS TRP GLY SER          
SEQRES  22 B  325  GLN SER GLU ASN ARG PRO SER PHE GLN ASP CYS GLU PRO          
SEQRES  23 B  325  LYS THR ASN GLU VAL TYR ASN LEU VAL LYS ASP LYS VAL          
SEQRES  24 B  325  ASP ALA ALA VAL SER GLU VAL LYS HIS TYR LEU SER GLN          
SEQRES  25 B  325  HIS LEU GLU HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS          
FORMUL   3  HOH   *106(H2 O)                                                    
HELIX    1   1 SER A   18  GLU A   20  5                                   3    
HELIX    2   2 ASN A   54  VAL A   66  1                                  13    
HELIX    3   3 SER A  102  GLN A  108  5                                   7    
HELIX    4   4 PRO A  114  SER A  134  1                                  21    
HELIX    5   5 LYS A  145  SER A  147  5                                   3    
HELIX    6   6 GLY A  186  LEU A  191  5                                   6    
HELIX    7   7 ASP A  192  LEU A  196  5                                   5    
HELIX    8   8 SER A  204  GLY A  222  1                                  19    
HELIX    9   9 PRO A  246  LEU A  250  5                                   5    
HELIX   10  10 GLY A  259  TRP A  271  1                                  13    
HELIX   11  11 GLN A  274  ARG A  278  5                                   5    
HELIX   12  12 SER A  280  LYS A  296  1                                  17    
HELIX   13  13 LYS A  298  SER A  311  1                                  14    
HELIX   14  14 SER B   18  GLU B   20  5                                   3    
HELIX   15  15 LYS B   57  VAL B   66  1                                  10    
HELIX   16  16 LEU B  103  LEU B  107  5                                   5    
HELIX   17  17 PRO B  114  SER B  134  1                                  21    
HELIX   18  18 LYS B  145  SER B  147  5                                   3    
HELIX   19  19 ASP B  192  PHE B  197  5                                   6    
HELIX   20  20 SER B  204  GLY B  222  1                                  19    
HELIX   21  21 PRO B  246  LEU B  250  5                                   5    
HELIX   22  22 GLY B  259  TRP B  271  1                                  13    
HELIX   23  23 GLN B  274  ARG B  278  5                                   5    
HELIX   24  24 SER B  280  LYS B  296  1                                  17    
HELIX   25  25 LYS B  298  SER B  311  1                                  14    
SHEET    1   A 6 LEU A  16  VAL A  17  0                                        
SHEET    2   A 6 GLY A  78  THR A  80  1  O  VAL A  79   N  VAL A  17           
SHEET    3   A 6 VAL A  88  ARG A  96 -1  O  VAL A  94   N  GLY A  78           
SHEET    4   A 6 HIS A  46  VAL A  53 -1  N  ALA A  49   O  THR A  95           
SHEET    5   A 6 VAL A  35  HIS A  41 -1  N  PHE A  37   O  VAL A  50           
SHEET    6   A 6 LEU A  22  LYS A  30 -1  N  GLU A  26   O  ARG A  38           
SHEET    1   B 4 LEU A  16  VAL A  17  0                                        
SHEET    2   B 4 GLY A  78  THR A  80  1  O  VAL A  79   N  VAL A  17           
SHEET    3   B 4 VAL A  88  ARG A  96 -1  O  VAL A  94   N  GLY A  78           
SHEET    4   B 4 LEU A  83  TRP A  85 -1  N  LEU A  83   O  GLY A  90           
SHEET    1   C 2 LEU A 139  LEU A 140  0                                        
SHEET    2   C 2 THR A 166  PHE A 167 -1  O  THR A 166   N  LEU A 140           
SHEET    1   D 2 ILE A 149  LEU A 151  0                                        
SHEET    2   D 2 ALA A 157  LEU A 159 -1  O  LYS A 158   N  LEU A 150           
SHEET    1   E 6 LEU B  16  VAL B  17  0                                        
SHEET    2   E 6 GLY B  78  THR B  80  1  O  VAL B  79   N  VAL B  17           
SHEET    3   E 6 VAL B  88  ARG B  96 -1  O  VAL B  94   N  GLY B  78           
SHEET    4   E 6 HIS B  46  VAL B  53 -1  N  VAL B  53   O  GLN B  91           
SHEET    5   E 6 GLY B  34  HIS B  41 -1  N  PHE B  37   O  VAL B  50           
SHEET    6   E 6 LEU B  22  GLY B  29 -1  N  GLU B  26   O  ARG B  38           
SHEET    1   F 4 LEU B  16  VAL B  17  0                                        
SHEET    2   F 4 GLY B  78  THR B  80  1  O  VAL B  79   N  VAL B  17           
SHEET    3   F 4 VAL B  88  ARG B  96 -1  O  VAL B  94   N  GLY B  78           
SHEET    4   F 4 LEU B  83  TRP B  85 -1  N  TRP B  85   O  VAL B  88           
SHEET    1   G 2 LEU B 139  LEU B 140  0                                        
SHEET    2   G 2 THR B 166  PHE B 167 -1  O  THR B 166   N  LEU B 140           
SHEET    1   H 2 ILE B 149  LEU B 151  0                                        
SHEET    2   H 2 ALA B 157  LEU B 159 -1  O  LYS B 158   N  LEU B 150           
CISPEP   1 ASP A  136    PRO A  137          0        -0.50                     
CISPEP   2 ASP B  136    PRO B  137          0         0.94                     
CRYST1  155.224   51.634  107.288  90.00 132.99  90.00 C 1 2 1       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006442  0.000000  0.006006        0.00000                         
SCALE2      0.000000  0.019367  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012743        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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